基异构酶和光活性黄色蛋白在整个活性位点的结构合网络
Journal of the American Chemical Society
|July 11, 2018
概括
蛋白质网络中的键结构上是合的,一个键的变化会影响其他键. 在多种蛋白质中观察到的这种合表明了生物系统的基本特性.
科学领域:
- 生物化学
- 结构生物学
- 蛋白质动力学
背景情况:
- 键在生物系统中形成关键网络,影响蛋白质折叠,识别,催化和化.
- 这些键网络中的结构合尚未完全理解.
研究的目的:
- 研究蛋白质网络中的键之间的结构合的程度和性质.
- 要确定一个键的扰动是否会影响网络中的其他键.
主要方法:
- 研究了三种蛋白质系统:两种类型的类异构酶和光活性黄色蛋白.
- 使用定位突变和非自然氨基酸替代来扰乱键网络.
- 使用1H核磁共振和高分辨率X射线晶体学来测量键长度的变化.
主要成果:
- 扰乱一个氧化离子孔会对另一个产生反作用.
- 远距离的键也影响了氧离子孔键,更紧密的键的影响更大.
- 在三种系统中的19次测量中观察到0.30±0.03的一致合系数.
- 分子力学和QM/MM计算重现了近距离合,而QM/MM则需要用于远距离效应,突出显示了极化作用.
结论:
- 蛋白质网络中的键表现出显著的结构合,即使在很长的距离.
- 这种合似乎受到周围蛋白质支架的最小影响.
- 这些发现提供了适用于新系统的键合的定量关系,并表明了这些相互作用中的极化的重要性.
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